ID   ATPD_AGABI              Reviewed;         162 AA.
AC   Q92196;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial;
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   Name=atpD;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Horst U1;
RX   PubMed=9202475; DOI=10.1099/00221287-143-6-1993;
RA   De Groot P.W.J., Schaap P.J., Van Griensven L.J.L.D., Visser J.;
RT   "Isolation of developmentally regulated genes from the edible mushroom
RT   Agaricus bisporus.";
RL   Microbiology 143:1993-2001(1997).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core, and
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP turnover in
CC       the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; Z82020; CAB04785.1; -; mRNA.
DR   AlphaFoldDB; Q92196; -.
DR   SMR; Q92196; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
PE   2: Evidence at transcript level;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transit peptide; Transport.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..162
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002666"
SQ   SEQUENCE   162 AA;  17364 MW;  533DC53B6C264112 CRC64;
     MSSLRLLASA ARRATTHVAY TRRGYAEISD KLKLSLALPH KAIFSSQDVV QVNIPAESGD
     MGILSSHVPS IEPLRPGVVE VVEDSGSQKW FVSGGFATVH PNNRLTINVV EAAPLEDFSI
     EAIRANLQEA NKVAAGSGSE ADKMEAQIEA EVYEALQHAL AK